ID A0A1D8PPE2_CANAL Unreviewed; 619 AA.
AC A0A1D8PPE2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Fet31p {ECO:0000313|EMBL:AOW29996.1};
GN Name=FET31 {ECO:0000313|CGD:CAL0000197324,
GN ECO:0000313|EMBL:AOW29996.1};
GN OrderedLocusNames=CAALFM_C600480CA {ECO:0000313|EMBL:AOW29996.1},
GN orf19.11687 {ECO:0000313|CGD:CAL0000197324};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW29996.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW29996.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2] {ECO:0000313|EMBL:AOW29996.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3] {ECO:0000313|EMBL:AOW29996.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; CP017628; AOW29996.1; -; Genomic_DNA.
DR RefSeq; XP_711263.2; XM_706171.2.
DR AlphaFoldDB; A0A1D8PPE2; -.
DR SMR; A0A1D8PPE2; -.
DR STRING; 237561.A0A1D8PPE2; -.
DR EnsemblFungi; C6_00480C_A-T; C6_00480C_A-T-p1; C6_00480C_A.
DR GeneID; 3647151; -.
DR KEGG; cal:CAALFM_C600480CA; -.
DR CGD; CAL0000197324; FET31.
DR VEuPathDB; FungiDB:C6_00480C_A; -.
DR InParanoid; A0A1D8PPE2; -.
DR OMA; HWHGQHH; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0033573; C:high-affinity iron permease complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IBA:GO_Central.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR CDD; cd13851; CuRO_1_Fet3p; 1.
DR CDD; cd13877; CuRO_2_Fet3p_like; 1.
DR CDD; cd13899; CuRO_3_Fet3p; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR044130; CuRO_2_Fet3-like.
DR PANTHER; PTHR11709:SF361; IRON TRANSPORT MULTICOPPER OXIDASE FET3; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron transport {ECO:0000256|ARBA:ARBA00022496};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000559};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..619
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009111211"
FT TRANSMEM 557..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..145
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 153..299
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 361..500
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 619 AA; 70571 MW; F05FC96CE6716FEF CRC64;
MRSLSIFSLV FLFFSTLITA KTHTWYYKTG WVNANPDGGF ERPMIGFNDS WPLPTLRVKK
GDTVNLYLIN GFDDRNTSLH FHGLFQHGTN QMDGPEMVTQ CPIPPGETFL YNFTVDDQVG
SYWYHSHTSG QYGDGMRGVF IIEDDDFPYD YDEEVILTLG EHYHDFSDDL HKNFMSRYNP
TGAEPIPSNI LFNETRNNTW KVEPGKTYFV RIINIGRFVS QYVWMEDHEF TIVEVDGIYV
EKNTTDLIYI TVAQRYGVLI TTKNSTDKNY AFMNRVDIDM LDVIPDELEL NGTNYIEYNS
KADKPEPYLL DSIDDYFDDF YLKPLSKEKL LDDADYTITV DVQMDNLGNG VNYAFFNNIT
YTTPRVPTLL SVLSAGDDAS NELVYGTNTN SFVLQSGDVV DIVLNNLDTG KHPFHLHGHV
FQLIERHEEI PETEDPVGYN ASDHADWPEY PMLRDTVYVR PQSYIVMRFK ADNPGVWLFH
CHIEWHLDQG LAIQLIEDPQ GIQKNASQHI TDNHKQICEK VGVSWEGNAA ANSKDYLNLK
GENVQHKRLP TGFTARGIVA LVFSCIAGVL GLATIAYYGM NDIADVEERV ARDLDVDFDE
EDNEIVNEGS SSSGSNSKH
//
